Function of glutathione peroxidases in legume root nodules

Autores
Matamoros, Manuel A.; Saiz, Ana; Peñuelas, Maria; Bustos Sanmamed, Maria del Pilar; Mulet, Jose M.; Barja, Maria V.; Rouhier, Nicolas; Moore, Marten; James, Euan K.; Dietz, Karl Josef; Becana, Manuel
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Glutathione peroxidases (Gpxs) are antioxidant enzymes not studied so far in legume nodules, despite the fact that reactive oxygen species are produced at different steps of the symbiosis. The function of two Gpxs that are highly expressed in nodules of the model legume Lotus japonicus was examined. Gene expression analysis, enzymatic and nitrosylation assays, yeast cell complementation, in situ mRNA hybridization, immunoelectron microscopy, and LjGpx-green fluorescent protein (GFP) fusions were used to characterize the enzymes and to localize each transcript and isoform in nodules. The LjGpx1 and LjGpx3 genes encode thioredoxin-dependent phospholipid hydroperoxidases and are differentially regulated in response to nitric oxide (NO) and hormones. LjGpx1 and LjGpx3 are nitrosylated in vitro or in plants treated with S-nitrosoglutathione (GSNO). Consistent with the modification of the peroxidatic cysteine of LjGpx3, in vitro assays demonstrated that this modification results in enzyme inhibition. The enzymes are highly expressed in the infected zone, but the LjGpx3 mRNA is also detected in the cortex and vascular bundles. LjGpx1 is localized to the plastids and nuclei, and LjGpx3 to the cytosol and endoplasmic reticulum. Based on yeast complementation experiments, both enzymes protect against oxidative stress, salt stress, and membrane damage. It is concluded that both LjGpxs perform major antioxidative functions in nodules, preventing lipid peroxidation and other oxidative processes at different subcellular sites of vascular and infected cells. The enzymes are probably involved in hormone and NO signalling, and may be regulated through nitrosylation of the peroxidatic cysteine essential for catalytic function.
Fil: Matamoros, Manuel A.. Consejo Superior de Investigaciones Científicas; España
Fil: Saiz, Ana. Consejo Superior de Investigaciones Científicas; España
Fil: Peñuelas, Maria. Consejo Superior de Investigaciones Científicas; España
Fil: Bustos Sanmamed, Maria del Pilar. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Institut des Sciences du Végétal; Francia
Fil: Mulet, Jose M.. Consejo Superior de Investigaciones Científicas; España. Universidad Politécnica de Valencia; España
Fil: Barja, Maria V.. Consejo Superior de Investigaciones Científicas; España. Universidad Politécnica de Valencia; España
Fil: Rouhier, Nicolas. Universite de Lorraine; Francia. Institut National de la Recherche Agronomique; Francia
Fil: Moore, Marten. Bielefeld University; Alemania
Fil: James, Euan K.. The James Hutton Institute; Reino Unido
Fil: Dietz, Karl Josef. Bielefeld University; Alemania
Fil: Becana, Manuel. Consejo Superior de Investigaciones Científicas; España
Materia
Antioxidants
Glutathione Peroxidases
Legume Nodules
Lotus Japonicus
Nitric Oxide
Reactive Oxygen Species
S-Nitrosylation
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/51047
Acceder
id CONICETDig_e5b7684b8cd452680e2af9ab9fd4b0eb
oai_identifier_str oai:ri.conicet.gov.ar:11336/51047
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Function of glutathione peroxidases in legume root nodulesMatamoros, Manuel A.Saiz, AnaPeñuelas, MariaBustos Sanmamed, Maria del PilarMulet, Jose M.Barja, Maria V.Rouhier, NicolasMoore, MartenJames, Euan K.Dietz, Karl JosefBecana, ManuelAntioxidantsGlutathione PeroxidasesLegume NodulesLotus JaponicusNitric OxideReactive Oxygen SpeciesS-Nitrosylationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Glutathione peroxidases (Gpxs) are antioxidant enzymes not studied so far in legume nodules, despite the fact that reactive oxygen species are produced at different steps of the symbiosis. The function of two Gpxs that are highly expressed in nodules of the model legume Lotus japonicus was examined. Gene expression analysis, enzymatic and nitrosylation assays, yeast cell complementation, in situ mRNA hybridization, immunoelectron microscopy, and LjGpx-green fluorescent protein (GFP) fusions were used to characterize the enzymes and to localize each transcript and isoform in nodules. The LjGpx1 and LjGpx3 genes encode thioredoxin-dependent phospholipid hydroperoxidases and are differentially regulated in response to nitric oxide (NO) and hormones. LjGpx1 and LjGpx3 are nitrosylated in vitro or in plants treated with S-nitrosoglutathione (GSNO). Consistent with the modification of the peroxidatic cysteine of LjGpx3, in vitro assays demonstrated that this modification results in enzyme inhibition. The enzymes are highly expressed in the infected zone, but the LjGpx3 mRNA is also detected in the cortex and vascular bundles. LjGpx1 is localized to the plastids and nuclei, and LjGpx3 to the cytosol and endoplasmic reticulum. Based on yeast complementation experiments, both enzymes protect against oxidative stress, salt stress, and membrane damage. It is concluded that both LjGpxs perform major antioxidative functions in nodules, preventing lipid peroxidation and other oxidative processes at different subcellular sites of vascular and infected cells. The enzymes are probably involved in hormone and NO signalling, and may be regulated through nitrosylation of the peroxidatic cysteine essential for catalytic function.Fil: Matamoros, Manuel A.. Consejo Superior de Investigaciones Científicas; EspañaFil: Saiz, Ana. Consejo Superior de Investigaciones Científicas; EspañaFil: Peñuelas, Maria. Consejo Superior de Investigaciones Científicas; EspañaFil: Bustos Sanmamed, Maria del Pilar. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Institut des Sciences du Végétal; FranciaFil: Mulet, Jose M.. Consejo Superior de Investigaciones Científicas; España. Universidad Politécnica de Valencia; EspañaFil: Barja, Maria V.. Consejo Superior de Investigaciones Científicas; España. Universidad Politécnica de Valencia; EspañaFil: Rouhier, Nicolas. Universite de Lorraine; Francia. Institut National de la Recherche Agronomique; FranciaFil: Moore, Marten. Bielefeld University; AlemaniaFil: James, Euan K.. The James Hutton Institute; Reino UnidoFil: Dietz, Karl Josef. Bielefeld University; AlemaniaFil: Becana, Manuel. Consejo Superior de Investigaciones Científicas; EspañaOxford University Press2015-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/51047Matamoros, Manuel A.; Saiz, Ana; Peñuelas, Maria; Bustos Sanmamed, Maria del Pilar; Mulet, Jose M.; et al.; Function of glutathione peroxidases in legume root nodules; Oxford University Press; Journal of Experimental Botany; 66; 10; 5-2015; 2979-29900022-0957CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1093/jxb/erv066info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jxb/article/66/10/2979/533365info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:50:21Zoai:ri.conicet.gov.ar:11336/51047instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:50:21.612CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Function of glutathione peroxidases in legume root nodules
title Function of glutathione peroxidases in legume root nodules
spellingShingle Function of glutathione peroxidases in legume root nodules
Matamoros, Manuel A.
Antioxidants
Glutathione Peroxidases
Legume Nodules
Lotus Japonicus
Nitric Oxide
Reactive Oxygen Species
S-Nitrosylation
title_short Function of glutathione peroxidases in legume root nodules
title_full Function of glutathione peroxidases in legume root nodules
title_fullStr Function of glutathione peroxidases in legume root nodules
title_full_unstemmed Function of glutathione peroxidases in legume root nodules
title_sort Function of glutathione peroxidases in legume root nodules
dc.creator.none.fl_str_mv Matamoros, Manuel A.
Saiz, Ana
Peñuelas, Maria
Bustos Sanmamed, Maria del Pilar
Mulet, Jose M.
Barja, Maria V.
Rouhier, Nicolas
Moore, Marten
James, Euan K.
Dietz, Karl Josef
Becana, Manuel
author Matamoros, Manuel A.
author_facet Matamoros, Manuel A.
Saiz, Ana
Peñuelas, Maria
Bustos Sanmamed, Maria del Pilar
Mulet, Jose M.
Barja, Maria V.
Rouhier, Nicolas
Moore, Marten
James, Euan K.
Dietz, Karl Josef
Becana, Manuel
author_role author
author2 Saiz, Ana
Peñuelas, Maria
Bustos Sanmamed, Maria del Pilar
Mulet, Jose M.
Barja, Maria V.
Rouhier, Nicolas
Moore, Marten
James, Euan K.
Dietz, Karl Josef
Becana, Manuel
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Antioxidants
Glutathione Peroxidases
Legume Nodules
Lotus Japonicus
Nitric Oxide
Reactive Oxygen Species
S-Nitrosylation
topic Antioxidants
Glutathione Peroxidases
Legume Nodules
Lotus Japonicus
Nitric Oxide
Reactive Oxygen Species
S-Nitrosylation
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Glutathione peroxidases (Gpxs) are antioxidant enzymes not studied so far in legume nodules, despite the fact that reactive oxygen species are produced at different steps of the symbiosis. The function of two Gpxs that are highly expressed in nodules of the model legume Lotus japonicus was examined. Gene expression analysis, enzymatic and nitrosylation assays, yeast cell complementation, in situ mRNA hybridization, immunoelectron microscopy, and LjGpx-green fluorescent protein (GFP) fusions were used to characterize the enzymes and to localize each transcript and isoform in nodules. The LjGpx1 and LjGpx3 genes encode thioredoxin-dependent phospholipid hydroperoxidases and are differentially regulated in response to nitric oxide (NO) and hormones. LjGpx1 and LjGpx3 are nitrosylated in vitro or in plants treated with S-nitrosoglutathione (GSNO). Consistent with the modification of the peroxidatic cysteine of LjGpx3, in vitro assays demonstrated that this modification results in enzyme inhibition. The enzymes are highly expressed in the infected zone, but the LjGpx3 mRNA is also detected in the cortex and vascular bundles. LjGpx1 is localized to the plastids and nuclei, and LjGpx3 to the cytosol and endoplasmic reticulum. Based on yeast complementation experiments, both enzymes protect against oxidative stress, salt stress, and membrane damage. It is concluded that both LjGpxs perform major antioxidative functions in nodules, preventing lipid peroxidation and other oxidative processes at different subcellular sites of vascular and infected cells. The enzymes are probably involved in hormone and NO signalling, and may be regulated through nitrosylation of the peroxidatic cysteine essential for catalytic function.
Fil: Matamoros, Manuel A.. Consejo Superior de Investigaciones Científicas; España
Fil: Saiz, Ana. Consejo Superior de Investigaciones Científicas; España
Fil: Peñuelas, Maria. Consejo Superior de Investigaciones Científicas; España
Fil: Bustos Sanmamed, Maria del Pilar. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Institut des Sciences du Végétal; Francia
Fil: Mulet, Jose M.. Consejo Superior de Investigaciones Científicas; España. Universidad Politécnica de Valencia; España
Fil: Barja, Maria V.. Consejo Superior de Investigaciones Científicas; España. Universidad Politécnica de Valencia; España
Fil: Rouhier, Nicolas. Universite de Lorraine; Francia. Institut National de la Recherche Agronomique; Francia
Fil: Moore, Marten. Bielefeld University; Alemania
Fil: James, Euan K.. The James Hutton Institute; Reino Unido
Fil: Dietz, Karl Josef. Bielefeld University; Alemania
Fil: Becana, Manuel. Consejo Superior de Investigaciones Científicas; España
description Glutathione peroxidases (Gpxs) are antioxidant enzymes not studied so far in legume nodules, despite the fact that reactive oxygen species are produced at different steps of the symbiosis. The function of two Gpxs that are highly expressed in nodules of the model legume Lotus japonicus was examined. Gene expression analysis, enzymatic and nitrosylation assays, yeast cell complementation, in situ mRNA hybridization, immunoelectron microscopy, and LjGpx-green fluorescent protein (GFP) fusions were used to characterize the enzymes and to localize each transcript and isoform in nodules. The LjGpx1 and LjGpx3 genes encode thioredoxin-dependent phospholipid hydroperoxidases and are differentially regulated in response to nitric oxide (NO) and hormones. LjGpx1 and LjGpx3 are nitrosylated in vitro or in plants treated with S-nitrosoglutathione (GSNO). Consistent with the modification of the peroxidatic cysteine of LjGpx3, in vitro assays demonstrated that this modification results in enzyme inhibition. The enzymes are highly expressed in the infected zone, but the LjGpx3 mRNA is also detected in the cortex and vascular bundles. LjGpx1 is localized to the plastids and nuclei, and LjGpx3 to the cytosol and endoplasmic reticulum. Based on yeast complementation experiments, both enzymes protect against oxidative stress, salt stress, and membrane damage. It is concluded that both LjGpxs perform major antioxidative functions in nodules, preventing lipid peroxidation and other oxidative processes at different subcellular sites of vascular and infected cells. The enzymes are probably involved in hormone and NO signalling, and may be regulated through nitrosylation of the peroxidatic cysteine essential for catalytic function.
publishDate 2015
dc.date.none.fl_str_mv 2015-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/51047
Matamoros, Manuel A.; Saiz, Ana; Peñuelas, Maria; Bustos Sanmamed, Maria del Pilar; Mulet, Jose M.; et al.; Function of glutathione peroxidases in legume root nodules; Oxford University Press; Journal of Experimental Botany; 66; 10; 5-2015; 2979-2990
0022-0957
CONICET Digital
CONICET
url http://hdl.handle.net/11336/51047
identifier_str_mv Matamoros, Manuel A.; Saiz, Ana; Peñuelas, Maria; Bustos Sanmamed, Maria del Pilar; Mulet, Jose M.; et al.; Function of glutathione peroxidases in legume root nodules; Oxford University Press; Journal of Experimental Botany; 66; 10; 5-2015; 2979-2990
0022-0957
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1093/jxb/erv066
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jxb/article/66/10/2979/533365
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842269026486583296
score 13.13397

Publicaciones similares